Lactose Permease: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Savannah Anderson, Ralf Stephan, Eran Hodis, David Canner, Michal Harel, Alexander Berchansky

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-===Function of Lactose Permease===
+''This page refers to a physical model based on [[1PV7]] by the Milwaukee School of Engineering Center for BioMolecular Modeling''
-[[Image:(image info)|left|(Caption)]]  Lactose Permease is a transmembrane protein that facilitates the passage of lactose across the phospholipid bi-layer of the cell membrane.  The transport mechanism used is an active co-transport that uses the inwardly directed H+ electrochemical gradient as its driving force.  As a result, the lactose is accompanied from the periplasm to the cytoplasm of the celll by an H+ proton.
+[[Image:(image info)|left|(Caption)]]===Function of Lactose Permease===
+Lactose Permease is a transmembrane protein that facilitates the passage of lactose across the phospholipid bi-layer of the cell membrane.  The transport mechanism used is an active co-transport that uses the inwardly directed H+ electrochemical gradient as its driving force.  As a result, the lactose is accompanied from the periplasm to the cytoplasm of the celll by an H+ proton.
 Lactose is a disaccharide carbohydrate found primarily in mammalian milk.  The disaccharide consists of the monosacharides glucose and galactose.  When the lactose is ingested and absorbed into the cell, the enzyme lactase breaks the disaccharide into its monosaccharide subunits.  These are in turn used in the cellular respiration process and broken down further into energy for the cell.
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 ===Structure of Lactose Permease===
 <applet load="1PV7" size="300" color="white" frame="true" align="right" caption="Lactose Permease" />
-<scene name='Lactose_Permease/Beginning/1'>Lactose permease</scene> is a transmembrane protein consisting of N- and C- terminal domains, each with six <scene name='Lactose_Permease/Backbone/1'>transmembrane helicies</scene> symmetrically positioned within the permease.  There are six sidechains that play an irreplaceable role in the active transport of lactose through the protien.  Three of these sidechains, <scene name='Lactose_Permease/Glu126/1'>Glutamic Acid 126</scene>, <scene name='Lactose_Permease/Arg144/1'>Arginine 144</scene>, and <scene name='Lactose_Permease/Glu269/1'>Glutamic Acid 269</scene> have been shown to be crucial in substrate binding activities.  <scene name='Lactose_Permease/Arg302/1'>Arginine 302</scene>, <scene name='Lactose_Permease/His322/1'>Histidine 322</scene>, and <scene name='Lactose_Permease/Glu325/1'>Glutamic Acid 325</scene> are known to play a significant role in proton translocation(moving the H+ proton) throughout the transport process.  Additionally, there are two residues that are suspected to play an important role in the alignment of the galactopyranosyl end of the substrate.  These are <scene name='Lactose_Permease/Cys148/1'>Cysteine 148</scene> and <scene name='Lactose_Permease/Trp151/1'>Tryptophan 151</scene>.
+<scene name='Lactose_Permease/Beginning/1'>Lactose permease</scene> is a transmembrane protein consisting of N- and C- terminal domains, each with six <scene name='Lactose_Permease/Backbone/1'>transmembrane helicies</scene> symmetrically positioned within the permease.  There are six sidechains that play an irreplaceable role in the active transport of lactose through the protein.  Three of these sidechains, <scene name='Lactose_Permease/Glu126/1'>Glutamic Acid 126</scene>, <scene name='Lactose_Permease/Arg144/1'>Arginine 144</scene>, and <scene name='Lactose_Permease/Glu269/1'>Glutamic Acid 269</scene> have been shown to be crucial in substrate binding activities.  <scene name='Lactose_Permease/Arg302/1'>Arginine 302</scene>, <scene name='Lactose_Permease/His322/1'>Histidine 322</scene>, and <scene name='Lactose_Permease/Glu325/1'>Glutamic Acid 325</scene> are known to play a significant role in proton translocation(moving the H+ proton) throughout the transport process.  Additionally, there are two residues that are suspected to play an important role in the alignment of the galactopyranosyl end of the substrate.  These are <scene name='Lactose_Permease/Cys148/1'>Cysteine 148</scene> and <scene name='Lactose_Permease/Trp151/1'>Tryptophan 151</scene>.
 These sidechains, which make up the active site of the protein, can be found within the large internal <scene name='Lactose_Permease/Cavity/1'>hydrophilic cavity</scene> of the lactose permease.  It is here where the <scene name='Lactose_Permease/Sugar/1'>substrate</scene> is recieved for transport and it is the location from which it is deposited into the cell.  The currently crystalized form of the permease is considered an 'inward-facing' conformation.  This implies that the hydrophilic cavity mentioned previously is positioned with the opening towards the cytoplasm of the cell.  Conversely, and outward-facing conformation would have the cavity facing the periplasm.